In general, biomacromolecules have superior affinity and selectivity for specific target materials in order to perform biological functions.
The most important factor in the activity of the biomacromolecules is the folded structure of peptides constituting the biomacromolecules. The folded structure, or the secondary structure, of the peptides can be stably controlled by maintaining specific environmental conditions. However, when the peptides are separated from the biomacromolecules (e.g., proteins), the peptides are unfolded as inactive random coils as the folded structure of the peptides is destabilized.
To solve this problem, there have been various studies aimed to stabilize the secondary structure of peptides for a long time without influence from surroundings. Most of these studies are about peptides with α-helix secondary structures which are the most frequently used among the biomacromolecules and have the most important activities.
As the most representative example of these studies, an invention of self-assembling peptides into cyclic molecules such that the α-helix secondary structures of the peptides are stabilized in the cycles has been presented.
The preparation of the cyclic peptides is limited in terms of commercialization due to the problems of a complicated process, low yield and difficult purification as compared to the synthesis of linear peptides. Furthermore, there is a fundamental limitation in that the peptide monomer has specificity for only one interaction and cannot target multiple interactions.
The inventors of present disclosure have made efforts to overcome the problems described above and provide a one-pot synthesis method for constructing a peptide with multiple α-helix secondary structures and have completed the present disclosure.